Rabellino Andrea, Andreani Cristina, Scaglioni Pier Paolo
Department of Internal Medicine, The University of Texas Southwestern Medical Center, Dallas, Texas.
Simmons Cancer Center, The University of Texas Southwestern Medical Center, Dallas, Texas.
Cancer Res. 2017 Apr 1;77(7):1542-1547. doi: 10.1158/0008-5472.CAN-16-2958. Epub 2017 Mar 22.
SUMOylation modifies the interactome, localization, activity, and lifespan of its target proteins. This process regulates several cellular machineries, including transcription, DNA damage repair, cell-cycle progression, and apoptosis. Accordingly, SUMOylation is critical in maintaining cellular homeostasis, and its deregulation leads to the corruption of a plethora of cellular processes that contribute to disease states. Among the proteins involved in SUMOylation, the protein inhibitor of activated STAT (PIAS) E3-ligases were initially described as transcriptional coregulators. Recent findings also indicate that they have a role in regulating protein stability and signaling transduction pathways. PIAS proteins interact with up to 60 cellular partners affecting several cellular processes, most notably immune regulation and DNA repair, but also cellular proliferation and survival. Here, we summarize the current knowledge about their role in tumorigenesis and cancer-related processes. .
小泛素样修饰(SUMOylation)可修饰其靶蛋白的相互作用组、定位、活性和寿命。这一过程调节多种细胞机制,包括转录、DNA损伤修复、细胞周期进程和细胞凋亡。因此,SUMOylation对于维持细胞稳态至关重要,其失调会导致大量导致疾病状态的细胞过程紊乱。在参与SUMOylation的蛋白质中,活化STAT蛋白抑制剂(PIAS)E3连接酶最初被描述为转录共调节因子。最近的研究结果还表明,它们在调节蛋白质稳定性和信号转导途径中发挥作用。PIAS蛋白可与多达60个细胞伴侣相互作用,影响多种细胞过程,最显著的是免疫调节和DNA修复,也包括细胞增殖和存活。在这里,我们总结了目前关于它们在肿瘤发生和癌症相关过程中作用的知识。